ArticleActa crystallographica. Section F, Structural biology communications2015
An active site-tail interaction in the structure of hexahistidine-tagged Thermoplasma acidophilum citrate synthase.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- The Encystment-Related MicroRNAs and Its Regulation Molecular Mechanism inInternational journal of molecular sciences · 2020Article
- ATP-citrate lyase multimerization is required for coenzyme-A substrate binding and catalysis.The Journal of biological chemistry · 2019Article
- Structural insights into the inhibition properties of archaeon citrate synthase from Metallosphaera sedula.PloS one · 2019Article
- Crystal Structures of Two Isozymes of Citrate Synthase from Sulfolobus tokodaii Strain 7.Biochemistry research international · 2016Article
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3 authors at 1 institution in 1 country.
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Abstract
Citrate synthase (CS) plays a central metabolic role in aerobes and many other organisms. The CS reaction comprises two half-reactions: a Claisen aldol condensation of acetyl-CoA (AcCoA) and oxaloacetate (OAA) that forms citryl-CoA (CitCoA), and CitCoA hydrolysis. Protein conformational changes that `close' the active site play an important role in the assembly of a catalytically competent condensation active site. CS from the thermoacidophile Thermoplasma acidophilum (TpCS) possesses an endogenous Trp fluorophore that can be used to monitor the condensation reaction. The 2.2 Å resolution crystal structure of TpCS fused to a C-terminal hexahistidine tag (TpCSH6) reported here is an `open' structure that, when compared with several liganded TpCS structures, helps to define a complete path for active-site closure. One active site in each dimer binds a neighboring His tag, the first nonsubstrate ligand known to occupy both the AcCoA and OAA binding sites. Solution data collectively suggest that this fortuitous interaction is stabilized by the crystalline lattice. As a polar but almost neutral ligand, the active site-tail interaction provides a new starting point for the design of bisubstrate-analog inhibitors of CS.
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